DNAJC6: A Potential Drug Target and Biomarker for DNA Damage Response and Cellular Stress

Target Name: DNAJC6

NCBI ID: G9829

DNAJC6

DNAJC6: A Potential Drug Target and Biomarker for DNA Damage Response and Cellular Stress

Introduction

DNA damage response (DR) is a critical cellular process that ensures the integrity of genetic information. DNA double-strand breaks (DSBs) can occur due to various factors, including aging, radiation, and mutations. The DNAJC6 protein is a member of the DNAJC6 (DnaJ heat shock protein family) and is involved in the cellular response to DNA damage. It plays a crucial role in the regulation of DNA repair and cell survival following DNA damage. In this article, we will discuss DNAJC6 as a drug target and biomarker for diseases associated with DNA damage.

Understanding DNAJC6

DNAJC6 is a 21-kDa protein that contains a N-terminal alpha-helix, a central 尾-sheet, and a C-terminal T-loop. It is a heat-shock protein that can be expressed in a variety of cell types, including bacteria, yeast, plants, and animals. DNAJC6 is highly conserved across different species, with similar or identical sequences in orthologous genes.

DNAJC6 functions as a molecular chaperone, helping to facilitate the transfer of DNA damage to the damaged strand. It also plays a role in the regulation of DNA repair by promoting the recruitment of repair factors to the site of DNA damage.

Mutations in DNAJC6 genes have been implicated in various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. Therefore, targeting DNAJC6 as a drug or biomarker could provide new insights into the development and treatment of these diseases.

Potential Drug Targets

Several studies have identified potential drug targets for DNAJC6. One of the most promising targets is the N-terminal domain of DNAJC6, which contains a unique GXXGXXE sequence. This sequence is highly conserved across different species and has been implicated in various cellular processes, including cell signaling, DNA binding, and protein-protein interactions.

N-terminal domain inhibitors have been shown to be effective in inhibiting the activity of DNAJC6, particularly in cell lines and animal models of cancer. These inhibitors can disrupt the protein-protein interaction between DNAJC6 and its downstream targets, leading to a reduction in the levels of DNAJC6 and its downstream targets.

Another potential drug target for DNAJC6 is the C-terminal domain. The C-terminal domain is involved in the regulation of DNAJC6 stability and has been shown to play a role in the interaction between DNAJC6 and its downstream targets.

Biomarkers

DNAJC6 has also been identified as a potential biomarker for diseases associated with DNA damage. The protein is expressed in a variety of cell types and can be used as a protein biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

One of the most promising applications of DNAJC6 as a biomarker is its ability to be used as a diagnostic marker for cancer. Several studies have shown that DNAJC6 is overexpressed in various types of cancer, including breast, ovarian, and colorectal cancers. Therefore, DNAJC6 has potential as a diagnostic marker for cancer and could be used in combination with other biomarkers for improved diagnostic accuracy.

Another application of DNAJC6 as a biomarker is its ability to be used as a target for small molecule inhibitors. The N-terminal domain of DNAJC6 is a potential target for small molecule inhibitors, and several studies have shown that inhibitors of this domain have the potential to inhibit the activity of DNAJC6. Therefore, DNAJC6 could be a valuable target for small molecule inhibitors in cancer and other diseases associated with DNA damage.

Conclusion

In conclusion, DNAJC6 is a protein involved in the DNA damage response and has

Protein Name: DnaJ Heat Shock Protein Family (Hsp40) Member C6

Functions: Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles. Plays a role in clathrin-mediated endocytosis in neurons (By similarity)

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